Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

F8DRV7 (F8DRV7_LACRS) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL AEI57509.1
Ordered Locus Names:HMPREF0538_21299 EMBL AEI57509.1
OrganismLactobacillus reuteri (strain ATCC 55730 / SD2112) [Complete proteome] [HAMAP] EMBL AEI57509.1
Taxonomic identifier491077 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus ›

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01039 RuleBase RU004512

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 SAAS SAAS005952 RuleBase RU004512

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 RuleBase RU004512

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS005952
   Molecular functionIsomerase SAAS SAAS005952 HAMAP-Rule MF_01039 EMBL AEI57509.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
F8DRV7 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 713FD0E21EDF9222

FASTA22826,122
        10         20         30         40         50         60 
MAKLVLIRHG QSEWNLSNQF TGWVDVDLSE KGVEQAKNAG KALKEHGIEF DYAYTSVLKR 

        70         80         90        100        110        120 
AIKTLHYALE ECDQLWIPEY KTWRLNERHY GALQGHNKQK AAEKYGDEQV HIWRRSYDVL 

       130        140        150        160        170        180 
PPLLSADDEG SAAKDRRYAN LDPRAIPGGE NLKVTLERVI PLWQDEIAPK LLDNKNVIIA 

       190        200        210        220 
AHGNSLRALS KYIENISDED IMNLEMATGQ PVVYDFDDKL NVLSKEKY

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002844 Genomic DNA. Translation: AEI57509.1.
RefSeqYP_004649799.1. NC_015697.1.

3D structure databases

ProteinModelPortalF8DRV7.
SMRF8DRV7. Positions 1-225.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI57509; AEI57509; HMPREF0538_21299.
GeneID10867345.
KEGGlru:HMPREF0538_21299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycLREU491077:GH1M-1347-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF8DRV7_LACRS
AccessionPrimary (citable) accession number: F8DRV7
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: February 19, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info